Abstract: An assay and kit for detecting N-retinylidene-N-retinylethanolamine (A2E) in a sample that uses a lipid binding protein, such as Saposin B, to capture A2E in the sample and assist in the extraction and measurement of A2E via mass spectroscopy. A2E thus serves as a marker for macular degeneration so that the assay and kit of the invention can be used to detect the presence or severity of macular degeneration.

Abstract: The invention pertains to a method for directly determining the biological activity of a Neurotoxin polypeptide in cells, comprising the steps of: a) incubating cells susceptible to Neurotoxin intoxication with a Neurotoxin polypeptide for a time and under conditions which allow for the Neurotoxin polypeptide to exert its biological activity; b) fixing the cells and, optionally, permeabilizing the cells with a detergent; c) contacting the cells with at least a first capture antibody specifically binding to the non-cleaved and Neurotoxin-cleaved substrate and with at least a second capture antibody specifically binding to the cleavage site of the Neurotoxin-cleaved substrate, under conditions which allow for binding of the capture antibodies to the substrates; d) contacting the cells with at least a first detection antibody specifically binding to the first capture antibody, under conditions which allow for binding of the first detection antibody to the first capture antibody, thus forming first detection comp

Abstract: Disclosed are systems and methods for selecting biological particles (e.g., cells or nuclei) based on specific binding to a substrate and single-biological particle measurement of analytes from the substrate-bound biological particles (e.g., cells or nuclei). Single biological particles (e.g., cells or nuclei) from a population of biological particles are captured through their binding to biological particle- (e.g., cell- or nucleus-) and/or molecule-specific biological particle (e.g., cell or nucleus) capture moieties on a substrate. Analytes are released from the single captured biological particles (e.g., cells or nuclei) and bind to analyte-specific barcode molecules associated with the specific biological particle (e.g., cell or nucleus) capture moieties to which a biological particle (e.g., a cell or nucleus) has bound. Analysis of the barcode molecules identifies the bound analytes.

Abstract: Compositions and methods for detection of anti-citrullinated protein antibodies (ACPAs) in rheumatoid arthritis (RA) patients. Patient samples known or suspected of containing ACPAs were probed against citrullinated proteins, and antibody responses to 190 citrullinated proteins in 20 RA patients were investigated. Unique antibody reactivity patterns in both clinical anti-cyclic citrullinated peptide assay positive (CCP+) and negative (CCP?) RA patients were observed. At individual antigen levels, six novel antibody/antigen complexes were discovered and validated against specific citrullinated antigens (Myelin Basic Protein (MBP), osteopontin (SPP1), flap endonuclease (FENI), insulin like growth factor binding protein 6 (IGFBP6), insulin like growth factor I (IGF1) and stanniocalcin-2 (STC2)) in RA patients. Identification of immune-dominant epitope(s) for citrullinated MBP was also performed. The identified biomarkers have high specificity, especially MBP.

Abstract: A recombinant, synthetic or monoclonal human antibody or fragment thereof that binds to an N-methyl-D-aspartate Receptor (NMDAR) epitope, which antibody or fragment comprises at least one a heavy chain variable domain sequence encoded by a nucleic acid sequence that is at least 80% identical to SEQ ID NOs. 1, 3, or 5; or at least one a light chain variable domain sequence encoded by a nucleic acid sequence that is at least 80% identical to SEQ ID NOs: 2, 4, or 6. Assays for diagnosis of ANRE employ these NMDAR-binding antibodies, constructs, or epitope binding fragments. In one embodiment, multiple of the NMDAR-binding antibodies or fragments are used as controls because they bind non-overlapping target sequences on the NMDAR ATD.

Abstract: It is an object of the present invention to provide a combination of a functional assessment of renal function together with biomarker results in order to improve assessment of patient at risk of, or having, an acute kidney injury. A loop diuretic such as furosemide inhibits luminal active chloride transport throughout the thick ascending limb of Henle, thereby preventing sodium reabsorption and resulting in natriuresis and increased urine flow. Loop diuretic-induced increases in urine output might be a method to assess the integrity of the renal tubular function in the setting of early AKI, and so a kidney's response, or lack thereof, to a diuretic challenge as a clinical assessment of tubular function can identify patients with severe tubular injury before it is clinically apparent (e.g. a rise in creatinine).

Abstract: The present invention relates to the chromatographic isolation of a target cell or another complex biological material, in particular by column chromatography such as affinity chromatography or gel permeation chromatography. The invention employs a receptor binding reagent that binds to a receptor molecule that is located on the surface of a target cell. The invention in general provides novel methods for the traceless isolation of biologic materials such as cells, cell organelles, viruses and the like. The invention also relates to an apparatus for the isolation of cells and other complex biological materials.

Abstract: The invention provides methods and compositions for distinguishing breast cancer.

Abstract: The present invention relates to a system for biodetection applications comprising two basic elements, a substrate with a functionalized surface and a nanoparticle, the system being capable of enhancing the plasmonic effect of the nanoparticle. The invention also relates to a biosensor incorporating such system, in addition to the method for detecting and quantifying a target analyte selected in a sample using such system. Finally, the invention relates to a device which can detect the enhanced optoplasmonic effect of the nanoparticles by means of the system of the invention or by combining the detection of such optoplasmonic effect with the analysis of the changes in the mechanical characteristics in the substrate.

Abstract: The present invention relates to the chromatographic isolation of a target cell or another complex biological material, in particular by column chromatography such as affinity chromatography or gel permeation chromatography. The invention employs a receptor binding reagent that binds to a receptor molecule that is located on the surface of a target cell. The invention in general provides novel methods for the traceless isolation of biologic materials such as cells, cell organelles, viruses and the like. The invention also relates to an apparatus for the isolation of cells and other complex biological materials.

Abstract: The present invention is to provide a method of exosome analysis that can analyze exosome in a sample in a simple manner. The method of exosome analysis of the present invention is a method of analyzing exosome in a sample, including: an addition step of adding a first antibody that specifically binds to a first antigen contained in the exosome and a second antibody that specifically binds to a second antigen contained in the exosome to the sample; a reaction step of causing the first antigen to be reacted with the first antibody and the second antigen to be reacted with the second antibody; and a detection step of detecting a reaction between the first antigen and the first antibody and a reaction between the second antigen and the second antibody.

Abstract: Provided is a monoclonal antibody or a fragment thereof in which heavy-chain complementarity-determining regions (CDRs) 1 to 3 respectively consist of amino acid sequences of SEQ ID NOs: 2 to 4 and light-chain CDRs 1 to 3 respectively consist of amino acid sequences of SEQ ID NOs: 5 to 7; a monoclonal antibody or a fragment thereof in which heavy-chain CDRs 1 to 3 respectively consist of amino acid sequences obtained by deleting, substituting, or adding one or several amino acids in the amino acid sequences of SEQ ID NOs: 2 to 4 and light-chain CDRs 1 to 3 respectively consist of amino acid sequences obtained by deleting, substituting, or adding one or several amino acids in the amino acid sequences of SEQ ID NOs: 5 to 7, and which has binding properties to a KK-LC-1 protein; or a monoclonal antibody or a fragment thereof which competes with the monoclonal antibody or a fragment thereof in which the heavy-chain CDRs 1 to 3 respectively consist of the amino acid sequences of SEQ ID NOs: 2 to 4 and the light-ch

Abstract: The present invention pertains to a method for directly determining the biological activity of a Neurotoxin polypeptide in cells, comprising the steps of: a) incubating cells susceptible to Neurotoxin intoxication with a Neurotoxin polypeptide for a time and under conditions which allow for the Neurotoxin polypeptide to exert its biological activity; b) fixing the cells and, optionally, permeabilizing the cells with a detergent; c) contacting the cells with at least a first capture antibody specifically binding to the non-cleaved and Neurotoxin-cleaved substrate and with at least a second capture antibody specifically binding to the cleavage site of the Neurotoxin-cleaved substrate, under conditions which allow for binding of said capture antibodies to said substrates; d) contacting the cells with at least a first detection antibody specifically binding to the first capture antibody, under conditions which allow for binding of said first detection antibody to said first capture antibody, thus forming first de

Abstract: The invention provides anti-variant Fc-region antibodies which specifically bind to an antibody that has the mutation P329G or the mutations P329G/L234A/L235A or the mutations 1253A/H310A/H435A in the Fc-region, and methods of using the same.

Abstract: Systems, methods, and devices for selective capture and release of target particles, e.g., living cells, from liquid samples, e.g., blood, are provided. The particle capture systems include a substrate; a first layer of gelatin bound to the substrate by physical adsorption, wherein the gelatin is functionalized with a plurality of first members of a binding pair; a second layer of gelatin wherein the gelatin is functionalized with a plurality of the first members of the binding pair and the second layer is bound to the first layer via a plurality of second members of the binding pair that are associated with the first members of the binding pair on both the first and the second layers; and a plurality of nanostructures bound to the second members of the binding pair and to one or more particle-binding moieties that selectively bind to the target particles.

Abstract: The present invention generally relates to method for preparing a biological sample for use in an immunolabeling process. The invention also relates to corresponding kits for use in the immunolabeling process.

Abstract: Methods and compositions are described for the diagnosis of primary biliary cirrhosis. Novel autoantigens are described for use in assays which employ test samples from individuals.

Abstract: Methods and kits for diagnosing systemic lupus erythematosus (SLE) in a subject are provided. Particularly, the present invention relates to specific oligonucleotide antibody reactivities useful in diagnosing SLE in a subject.

Abstract: Indirect ELISAs to detect exposure to Felis catus gammaherpesvirus 1 (FcaGHV1) in domestic cats. These ELISAs detect feline serum antibodies to ORF52 and ORF38 of FcaGHV1. The ELISA assays are sensitive, specific, and adaptable for scale up use in high throughput diagnostics.

Abstract: The present disclosure is directed to antibody-linked immuno-sedimentation agent, the antibody being linked to a sedimentation agent by a non-antigen binding region of the antibody, and a method of isolating a target from a sample using the antibody-linked immuno-sedimentation agent. The methods involve forming a mixture including a sample with an antibody linked immuno-sedimentation agent and red blood cells under conditions sufficient to form red blood cell rouleaux and allow antibody-antigen binding.